amino acids and phospholipids

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19 Terms

1
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what is the structure of an amino acid

  • amine group

  • carboxyl group

  • r group

<ul><li><p>amine group</p></li><li><p>carboxyl group</p></li><li><p>r group </p></li></ul><p></p>
2
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what type of bonds do amino acids form?

peptide bond, condensation reaction, the reaction takes place in the ribosome

3
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what enzyme catalyses the reaction of amino acids?

protease enzyme

4
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what is primary structure?

the specific order of amino acids in a polypeptide

  • determined by the DNA sequence of the gene which codes for that polypeptide

5
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what is the secondary structure?

the shape of the chain caused by hydrogen bonds e.g alpha helix or the beta pleated sheet

6
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what is the tertiary structure?

further folding of the secondary structure - active site

7
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what is the quaternary structure?

how individual polypeptide subunits (chains) are arranged with each other to form a larger 3D molecule e.g haemoglobin

8
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what is a prosthetic group?

non-protein molecules forming part of the structure

  • proteins with a prosthetic group are called conjugated proteins

9
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what are non polar amino acids?

non polar amino acids have uncharged R groups. they are not attracted to water and are called hydrophobic

10
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what are disulfide bonds?

the covalent bonds between two sulfur molecules, these are relatively strong

11
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what are globular proteins?

  • globular proteins tend to have a spherical shape

  • they are soluble in water → they have hydrophilic amino acids on their surface

  • some roles include enzymes, hormones and oxygen carrying proteins

12
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what are fibrous proteins?

  • often play a structural role e.g bones or tendons

  • form long rope like molecules

  • large proportion of amino acids with hydrophobic R groups → insoluble in water

13
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what is the structure of haemoglobin?

  • globular protein with 4 polypeptide subunits

  • two are called alpha and two are called beta subunits

  • each subunit contains the prosthetic group haem which is an Fe2+ (conjugated protein)

  • this is where the oxygen binds, so one haemoglobin molecule can bind to four oxygen molecules

  • when one molecule of oxygen joins the quaternary structure changes slightly which makes it more easier for more oxygen to attach

14
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what is the structure of collagen?

  • found in skin, tendons and ligaments

  • polypeptide chains wrap tightly together to form a triple helix

  • every third amino acid is glycine - the R group of glycine is hydrogen - the smallest R group of any amino acid

  • the polypeptides can wrap very tightly around each other

  • hydrogen bonds form between the polypeptide chains

  • polypeptides also joined by strong crosslinks

  • large number of polypeptide helixes join together to form microfibrils and fibrils

  • the molecules are staggered so there are no weak spots

15
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what is the structure of keratin?

  • found in hair and fingernails

  • insoluble in water

  • consists of long stranded molecules

  • high proportion of the amino acid cysteine

  • cysteine is used to form disulfide bonds

16
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what is the structure of elastin?

  • long strands containing hydrophobic regions

  • found in skin and arteries

17
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describe the structure of a phospholipid

  • glycerol bonded to two fatty acids and a phosphate

  • the phosphate head is negatively charged and is polar (hydrophilic)

  • the tails are non polar and hydrophobic

  • the tails are joined to the phospholipid via ester bonds

  • the phosphate is joined via phosphoester bonds

18
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describe the structure of cholesterol

  • hydrophilic hydroxyl group

  • rest is hydrophobic

19
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what is the role of cholesterol?

  • controls membrane fluidity

  • contributes to stability